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Iron in PDB 3p3p: Factor Inhibiting Hif-1 Alpha in Complex with Notch 1 Fragment Mouse Notch (1997-2016) Peptide

Enzymatic activity of Factor Inhibiting Hif-1 Alpha in Complex with Notch 1 Fragment Mouse Notch (1997-2016) Peptide

All present enzymatic activity of Factor Inhibiting Hif-1 Alpha in Complex with Notch 1 Fragment Mouse Notch (1997-2016) Peptide:
1.14.11.16;

Protein crystallography data

The structure of Factor Inhibiting Hif-1 Alpha in Complex with Notch 1 Fragment Mouse Notch (1997-2016) Peptide, PDB code: 3p3p was solved by M.A.Mcdonough, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.15 / 2.60
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 86.336, 86.336, 146.450, 90.00, 90.00, 90.00
R / Rfree (%) 20.8 / 25.9

Iron Binding Sites:

The binding sites of Iron atom in the Factor Inhibiting Hif-1 Alpha in Complex with Notch 1 Fragment Mouse Notch (1997-2016) Peptide (pdb code 3p3p). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Factor Inhibiting Hif-1 Alpha in Complex with Notch 1 Fragment Mouse Notch (1997-2016) Peptide, PDB code: 3p3p:

Iron binding site 1 out of 1 in 3p3p

Go back to Iron Binding Sites List in 3p3p
Iron binding site 1 out of 1 in the Factor Inhibiting Hif-1 Alpha in Complex with Notch 1 Fragment Mouse Notch (1997-2016) Peptide


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Factor Inhibiting Hif-1 Alpha in Complex with Notch 1 Fragment Mouse Notch (1997-2016) Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe350

b:41.0
occ:1.00
 OD2 A:ASP201 1.9 39.2 1.0
O A:HOH1044 2.0 57.5 1.0
NE2 A:HIS199 2.2 38.8 1.0
O2 A:AKG1351 2.2 53.3 1.0
O5 A:AKG1351 2.2 44.4 1.0
NE2 A:HIS279 2.3 36.0 1.0
C1 A:AKG1351 2.9 52.6 1.0
C2 A:AKG1351 2.9 50.6 1.0
CG A:ASP201 2.9 40.1 1.0
CE1 A:HIS199 3.0 39.7 1.0
OD1 A:ASP201 3.2 40.1 1.0
CD2 A:HIS279 3.2 34.0 1.0
CD2 A:HIS199 3.2 39.5 1.0
CE1 A:HIS279 3.3 36.1 1.0
O A:HOH1002 4.0 36.1 1.0
O1 A:AKG1351 4.0 56.9 1.0
ND1 A:HIS199 4.2 38.7 1.0
O A:HOH1157 4.2 61.2 1.0
CZ2 A:TRP296 4.2 51.2 1.0
C3 A:AKG1351 4.2 51.5 1.0
CB A:ASP201 4.3 36.4 1.0
CG A:HIS199 4.3 38.4 1.0
CG A:HIS279 4.4 36.5 1.0
ND1 A:HIS279 4.4 37.0 1.0
CB B:ASN210 4.5 96.9 1.0
O B:HOH1020 4.6 65.5 1.0
CG B:ASN210 4.8 95.7 1.0
C4 A:AKG1351 4.9 55.2 1.0
CH2 A:TRP296 4.9 53.9 1.0
OD1 B:ASN210 5.0 96.0 1.0
N B:ASN210 5.0 97.5 1.0

Reference:

M.L.Coleman, M.A.Mcdonough, K.S.Hewitson, C.Coles, J.Mecinovic, M.Edelmann, K.M.Cook, M.E.Cockman, D.E.Lancaster, B.M.Kessler, N.J.Oldham, P.J.Ratcliffe, C.J.Schofield. Asparaginyl Hydroxylation of the Notch Ankyrin Repeat Domain By Factor Inhibiting Hypoxia-Inducible Factor J.Biol.Chem. V. 282 24027 2007.
ISSN: ISSN 0021-9258
PubMed: 17573339
Page generated: Sun Aug 4 17:23:08 2024

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